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CAZyme Information: FVEG_05942-t26_1-p1

You are here: Home > Sequence: FVEG_05942-t26_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Fusarium verticillioides
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium verticillioides
CAZyme ID FVEG_05942-t26_1-p1
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
516 CM000579.1|CGC2 56046.66 8.2721
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Fverticillioides7600 16240 334819 371 15869
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC - -

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
180536 PRK06347 2.19e-09 127 418 307 576
1,4-beta-N-acetylmuramoylhydrolase.
212030 LysM 3.27e-06 152 196 1 45
Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
180536 PRK06347 3.63e-06 302 496 247 434
1,4-beta-N-acetylmuramoylhydrolase.
180536 PRK06347 3.89e-06 246 496 344 576
1,4-beta-N-acetylmuramoylhydrolase.
212030 LysM 8.32e-06 390 434 1 45
Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
3.44e-275 1 516 1 409
4.33e-202 12 516 15 523
2.18e-173 1 514 1 505
1.92e-169 14 516 15 518
1.55e-168 14 516 15 518

PDB Hits      help

FVEG_05942-t26_1-p1 has no PDB hit.

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.30e-109 11 439 16 458
LysM domain-containing protein ARB_05157 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05157 PE=1 SV=1
6.17e-16 242 367 40 188
LysM domain-containing protein ARB_03438 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_03438 PE=3 SV=1
7.00e-16 377 515 256 407
LysM domain-containing protein ARB_01488 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_01488 PE=3 SV=1
1.35e-10 303 360 380 437
Probable peptidoglycan-N-acetylglucosamine deacetylase ARB_03699 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_03699 PE=1 SV=2
1.62e-09 30 200 357 536
LysM domain-containing protein ARB_00327 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_00327 PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.538399 0.461589

TMHMM  Annotations      help

There is no transmembrane helices in FVEG_05942-t26_1-p1.